ID HYAL3_PIG Reviewed; 419 AA. AC Q6RHW2; Q6S3P5; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 100. DE RecName: Full=Hyaluronidase-3; DE Short=Hyal-3; DE EC=3.2.1.35; DE AltName: Full=Hyaluronoglucosaminidase-3; DE Flags: Precursor; GN Name=HYAL3; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=15218248; DOI=10.1159/000078571; RA Gatphayak K., Knorr C., Beck J., Brenig B.; RT "Molecular characterization of porcine hyaluronidase genes 1, 2, and 3 RT clustered on SSC13q21."; RL Cytogenet. Genome Res. 106:98-106(2004). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 127-247. RX PubMed=14619892; DOI=10.1159/000074181; RA Gatphayak K., Knorr C., Habermann F., Fries R., Brenig B.; RT "Assignment of the porcine hyaluronidase-3 (HYAL3) gene to SSC13-->q21 by RT FISH and confirmation by hybrid panel analyses."; RL Cytogenet. Genome Res. 101:178-178(2003). CC -!- FUNCTION: Facilitates sperm penetration into the layer of cumulus cells CC surrounding the egg by digesting hyaluronic acid. Involved in induction CC of the acrosome reaction in the sperm. Involved in follicular atresia, CC the breakdown of immature ovarian follicles that are not selected to CC ovulate. Induces ovarian granulosa cell apoptosis, possibly via CC apoptotic signaling pathway involving CASP8 and CASP3 activation, and CC poly(ADP-ribose) polymerase (PARP) cleavage. Has no hyaluronidase CC activity in embryonic fibroblasts in vitro. Has no hyaluronidase CC activity in granulosa cells in vitro. {ECO:0000250|UniProtKB:Q8VEI3}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D- CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; CC Evidence={ECO:0000250|UniProtKB:Q8VEI3}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VEI3}. Cell CC membrane {ECO:0000250|UniProtKB:Q8VEI3}. Cytoplasmic vesicle, secretory CC vesicle, acrosome {ECO:0000250|UniProtKB:Q8VEI3}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q8VEI3}. Early endosome CC {ECO:0000250|UniProtKB:Q8VEI3}. Note=Mostly present in low-density CC vesicles. Low levels in higher density vesicles of late endosomes and CC lysosomes. Localized in punctate cytoplasmic vesicles and in CC perinuclear structures, but does not colocalize with LAMP1. Localized CC on the plasma membrane over the acrosome and on the surface of the CC midpiece of the sperm tail. {ECO:0000250|UniProtKB:Q8VEI3}. CC -!- TISSUE SPECIFICITY: Highly expressed in bladder, spleen and liver. CC Expressed at low levels in the kidney. {ECO:0000269|PubMed:15218248}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8VEI3}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY497545; AAR91601.1; -; mRNA. DR EMBL; AY472019; AAR33037.1; -; Genomic_DNA. DR RefSeq; NP_999604.1; NM_214439.1. DR AlphaFoldDB; Q6RHW2; -. DR SMR; Q6RHW2; -. DR STRING; 9823.ENSSSCP00000052110; -. DR CAZy; GH56; Glycoside Hydrolase Family 56. DR GlyCosmos; Q6RHW2; 2 sites, No reported glycans. DR PaxDb; 9823-ENSSSCP00000012156; -. DR GeneID; 404696; -. DR KEGG; ssc:404696; -. DR CTD; 8372; -. DR eggNOG; ENOG502QTXP; Eukaryota. DR InParanoid; Q6RHW2; -. DR OrthoDB; 5344684at2759; -. DR BRENDA; 3.2.1.35; 6170. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB. DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB. DR GO; GO:0004415; F:hyalurononglucosaminidase activity; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB. DR GO; GO:2000355; P:negative regulation of ovarian follicle development; ISS:UniProtKB. DR GO; GO:0001552; P:ovarian follicle atresia; ISS:UniProtKB. DR GO; GO:0007341; P:penetration of zona pellucida; ISS:UniProtKB. DR GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; ISS:UniProtKB. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR018155; Hyaluronidase. DR InterPro; IPR027260; Hyaluronidase-3. DR PANTHER; PTHR11769; HYALURONIDASE; 1. DR PANTHER; PTHR11769:SF19; HYALURONIDASE-3; 1. DR Pfam; PF01630; Glyco_hydro_56; 1. DR PIRSF; PIRSF038193; Hyaluronidase; 1. DR PIRSF; PIRSF500776; Hyaluronidase_3; 1. DR PRINTS; PR00846; GLHYDRLASE56. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. PE 2: Evidence at transcript level; KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; EGF-like domain; KW Endoplasmic reticulum; Endosome; Fertilization; Glycoprotein; Glycosidase; KW Hydrolase; Membrane; Reference proteome; Secreted; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT CHAIN 17..419 FT /note="Hyaluronidase-3" FT /id="PRO_0000248202" FT DOMAIN 352..407 FT /note="EGF-like" FT ACT_SITE 129 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q12794" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 215 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 42..331 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 205..220 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 356..367 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 361..395 FT /evidence="ECO:0000250|UniProtKB:Q12794" FT DISULFID 397..406 FT /evidence="ECO:0000250|UniProtKB:Q12794" SQ SEQUENCE 419 AA; 46393 MW; 8035CDE3D04324AC CRC64; MTMQLGLALV LGVAMCLGCG QPLLRAPERP FCVLWNVPSA RCKARFGVHL PLEALGITAN HGQRFHGQNI TIFYKSQLGL YPYFGPRGTA HNGGIPQAVS LDHHLARAAY QIHRSLRPGF TGLAVLDWEE WCPLWAGNWG RRQAYQAASC AWAQRVYPNL DPQEQLCKAR AGFEEAARAL MEDTLRLGRM LRPHGLWGFY HYPACGNGWH GTASNYTGHC HAAALARNTQ LYWLWAASSA LFPSIYLPPG LPPAYHQAFV RYRLEEAFRV ALVGHPHPLP VLAYARLTHR NSGRFLSQDE LVQTIGVSAA LGASGVVLWG DLSFSSSEEE CWHLRGYLVG TLGPYVINVT RAAMACSHQR CHGHGRCAWQ DPGQLKVFLH LHPGGSPGAW ESFSCRCYWG WAGPTCQEPR PELGPEEAT //